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[Changes in hexokinase activity during muscle alteration].

V I Stabrovskaia, N F Krauzova, A D Braun

    Tsitologiia
    |October 1, 1984
    PubMed
    Summary
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    Heating and urea affect skeletal muscle hexokinase (HK) activity. Muscle heating initially decreases HK extractability and activity, while urea causes reversible activation, but irreversible inhibition occurs with prolonged exposure.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Muscle Physiology

    Background:

    • Hexokinase (HK) is a crucial enzyme in muscle energy metabolism.
    • Understanding enzyme stability under stress is vital for muscle function research.

    Purpose of the Study:

    • To investigate the effects of heat and urea on skeletal muscle hexokinase (HK) extractability and activity.
    • To examine the in vitro stability of HK in muscle extracts when exposed to heat and urea.

    Main Methods:

    • Skeletal muscles of Rana temporaria L. were subjected to controlled heating (37-42°C) and urea treatment (1-2 M).
    • Hexokinase (HK) extractability and activity were measured per gram of tissue and per milligram of protein.
    • In vitro stability assays of HK in muscle extracts were performed under similar conditions.

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    Main Results:

    • Heating muscle at 37°C decreased HK extractability and activity, with complete inhibition at 42°C.
    • In vitro heating of muscle extract reduced HK activity starting at 36°C.
    • Urea treatment at reversible alteration phases increased HK activity, but irreversible loss of muscle excitability correlated with complete HK activity loss.
    • In vitro, 1 M urea decreased HK activity to 67% within 30 minutes, with sustained reduction.

    Conclusions:

    • Skeletal muscle hexokinase (HK) is sensitive to thermal and chemical denaturation.
    • Urea-induced activation of HK may be linked to increased ATP content, suggesting complex regulatory mechanisms.
    • The differential effects of in vivo vs. in vitro urea treatment highlight the importance of cellular context in enzyme stability.